2M8U
Solution structure of the Dictyostelium discodieum Myosin Light Chain, MlcC
Summary for 2M8U
| Entry DOI | 10.2210/pdb2m8u/pdb |
| NMR Information | BMRB: 19274 |
| Descriptor | Myosin Light Chain, MlcC (1 entity in total) |
| Functional Keywords | myosin light chain, helical bundle, contractile protein |
| Biological source | Dictyostelium discoideum (Slime mold) |
| Total number of polymer chains | 1 |
| Total formula weight | 8917.95 |
| Authors | Liburd, J.D.,Miller, E.,Langelaan, D.,Chitayat, S.,Crawley, S.W.,Cote, G.P.,Smith, S.P. (deposition date: 2013-05-28, release date: 2014-12-24, Last modification date: 2024-05-15) |
| Primary citation | Langelaan, D.N.,Liburd, J.,Yang, Y.,Miller, E.,Chitayat, S.,Crawley, S.W.,Cote, G.P.,Smith, S.P. Structure of the Single-lobe Myosin Light Chain C in Complex with the Light Chain-binding Domains of Myosin-1C Provides Insights into Divergent IQ Motif Recognition. J.Biol.Chem., 291:19607-19617, 2016 Cited by PubMed Abstract: Myosin light chains are key regulators of class 1 myosins and typically comprise two domains, with calmodulin being the archetypal example. They bind IQ motifs within the myosin neck region and amplify conformational changes in the motor domain. A single lobe light chain, myosin light chain C (MlcC), was recently identified and shown to specifically bind to two sequentially divergent IQ motifs of the Dictyostelium myosin-1C. To provide a molecular basis of this interaction, the structures of apo-MlcC and a 2:1 MlcC·myosin-1C neck complex were determined. The two non-functional EF-hand motifs of MlcC pack together to form a globular four-helix bundle that opens up to expose a central hydrophobic groove, which interacts with the N-terminal portion of the divergent IQ1 and IQ2 motifs. The N- and C-terminal regions of MlcC make critical contacts that contribute to its specific interactions with the myosin-1C divergent IQ motifs, which are contacts that deviate from the traditional mode of calmodulin-IQ recognition. PubMed: 27466369DOI: 10.1074/jbc.M116.746313 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
